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7F8X

Crystal structure of the cholecystokinin receptor CCKAR in complex with NN9056

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. VSTwNLVAISLERYGaI
ChainResidueDetails
AVAL127-ILE143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
AALA42-ILE67

site_idSWS_FT_FI2
Number of Residues28
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AARG68-ASN77
AGLU138-HIS157

site_idSWS_FT_FI3
Number of Residues26
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
AILE78-LEU104

site_idSWS_FT_FI4
Number of Residues55
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
ALYS105-LYS115
ATYR179-HIS210
ATRP569-GLY583

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
ATHR116-LEU137

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
AALA158-ILE178

site_idSWS_FT_FI7
Number of Residues23
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
ATHR211-LEU234

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
AMET548-ALA568

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
ATHR584-MET607

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails
ACYS621

site_idSWS_FT_FI11
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN10
AASN24
AASN190

site_idSWS_FT_FI12
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU250

site_idSWS_FT_FI13
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP259

site_idSWS_FT_FI14
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU271
APHE478

site_idSWS_FT_FI15
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER491
AASN506

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU250proton shuttle (general acid/base)
AASP259covalent catalysis

219869

PDB entries from 2024-05-15

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